ID V3ZV56_LOTGI Unreviewed; 157 AA.
AC V3ZV56;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 03-MAY-2023, entry version 38.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
DE Flags: Fragment;
GN ORFNames=LOTGIDRAFT_86983 {ECO:0000313|EMBL:ESO88262.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO88262.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO88262.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR EMBL; KB202719; ESO88262.1; -; Genomic_DNA.
DR RefSeq; XP_009060949.1; XM_009062701.1.
DR AlphaFoldDB; V3ZV56; -.
DR STRING; 225164.V3ZV56; -.
DR EnsemblMetazoa; LotgiT86983; LotgiP86983; LotgiG86983.
DR GeneID; 20252714; -.
DR KEGG; lgi:LOTGIDRAFT_86983; -.
DR CTD; 20252714; -.
DR HOGENOM; CLU_029507_0_1_1; -.
DR OMA; YVNYGVT; -.
DR OrthoDB; 67394at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR029760; GPX_CS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR PANTHER; PTHR11592:SF133; GLUTATHIONE PEROXIDASE; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000499};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000499};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746}.
FT DOMAIN 1..157
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 34
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ESO88262.1"
FT NON_TER 157
FT /evidence="ECO:0000313|EMBL:ESO88262.1"
SQ SEQUENCE 157 AA; 18168 MW; 0241CCFEE66BFA03 CRC64;
DFYDFEVVDI HGNKVSLDEY RGMVTLVVNV ASECGYTDSH YKALIRLQNV LGKQNKFTVL
AFPCNQFGSQ EPGSREDIIT FTREKYHVNF PVFDKVNVLP PHVSEPWDYL IRKSGAAPNW
NFWKYLLDEN GQVLYSWGPW ASVEDIYKPI KEAVDKI
//
